Introduction

Tumor suppressor protein p53 plays an important role to maintain genomic integrity from cellular stress by trans-activating the target genes involved in different cellular functions, such as cell cycle arrest and apoptosis [
1]. The tetramer formation of p53 through the C-terminal tetramerization domain (TD) is essential for its activity. The p53 tetramerization domain consists of a b-strand (Glu326-333), a tight turn (Gly334), and an α-helix (Arg335-Gly356) (Fig.
1A). Approximately 50 % of human tumors carry inactivating mutations in the
p53 gene. To date, 41 point mutations have been found in 22 positions among 31 residues of the tetramerization domain (Fig.
1B). It is important to understand the mechanism of malignant transformation by mutations in the tetramerization domain [
2,
3].